BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
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Entry pathways of the pseudotype VSVs. Huh7 cells were pretreated with... | Download Scientific Diagram
PDF) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
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Endoplasmic Reticulum Protein Quality Control Is Determined by Cooperative Interactions between Hsp/c70 Protein and the CHIP E3 Ligase* - Journal of Biological Chemistry
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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. - Abstract - Europe PMC
The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast - Journal of Biological Chemistry
Frontiers | Impact of Chaperone-Mediated Autophagy in Brain Aging: Neurodegenerative Diseases and Glioblastoma | Frontiers in Aging Neuroscience
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PDF) A general approach for the synthesis of 5-substituted-4-amino-pyrrolidin-2-ones and 5-substituted-4-amino-3-pyrrolin-2-ones | Sergio Pinheiro - Academia.edu
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BAG‐1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release | The EMBO Journal
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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. - Abstract - Europe PMC
Timothée Beckmann (@timottimot) | Twitter
PDF) CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia
